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MULTISPECIES: bacterioferritin [Providencia]
bacterioferritin( domain architecture ID 10793432)
bacterioferritin regulates iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
PRK10635 | PRK10635 | bacterioferritin; Provisional |
1-158 | 1.79e-100 | |||
bacterioferritin; Provisional : Pssm-ID: 182604 Cd Length: 158 Bit Score: 285.19 E-value: 1.79e-100
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Name | Accession | Description | Interval | E-value | |||
PRK10635 | PRK10635 | bacterioferritin; Provisional |
1-158 | 1.79e-100 | |||
bacterioferritin; Provisional Pssm-ID: 182604 Cd Length: 158 Bit Score: 285.19 E-value: 1.79e-100
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Bacterioferritin | cd00907 | Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ... |
2-154 | 1.19e-84 | |||
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity. Pssm-ID: 153099 Cd Length: 153 Bit Score: 245.15 E-value: 1.19e-84
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Bfr | COG2193 | Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; |
3-154 | 1.10e-82 | |||
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; Pssm-ID: 441796 Cd Length: 152 Bit Score: 240.10 E-value: 1.10e-82
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bfr | TIGR00754 | bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ... |
1-157 | 1.55e-81 | |||
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 162022 Cd Length: 157 Bit Score: 237.40 E-value: 1.55e-81
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Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
8-143 | 1.64e-37 | |||
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins. Pssm-ID: 459712 Cd Length: 141 Bit Score: 125.09 E-value: 1.64e-37
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Name | Accession | Description | Interval | E-value | |||
PRK10635 | PRK10635 | bacterioferritin; Provisional |
1-158 | 1.79e-100 | |||
bacterioferritin; Provisional Pssm-ID: 182604 Cd Length: 158 Bit Score: 285.19 E-value: 1.79e-100
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Bacterioferritin | cd00907 | Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as ... |
2-154 | 1.19e-84 | |||
Bacterioferritin, ferritin-like diiron-binding domain; Bacterioferritins, also known as cytochrome b1, are members of a broad superfamily of ferritin-like diiron-carboxylate proteins. Similar to ferritin in architecture, Bfr forms an oligomer of 24 subunits that assembles to form a hollow sphere with 432 symmetry. Up to 12 heme cofactor groups (iron protoporphyrin IX or coproporphyrin III) are bound between dimer pairs. The role of the heme is unknown, although it may be involved in mediating iron-core reduction and iron release. Each subunit is composed of a four-helix bundle which carries a diiron ferroxidase center; it is here that initial oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of ferric-hydroxyphosphate at the core. Some bacterioferritins are composed of two subunit types, one conferring heme-binding ability (alpha) and the other (beta) bestowing ferroxidase activity. Pssm-ID: 153099 Cd Length: 153 Bit Score: 245.15 E-value: 1.19e-84
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Bfr | COG2193 | Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; |
3-154 | 1.10e-82 | |||
Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism]; Pssm-ID: 441796 Cd Length: 152 Bit Score: 240.10 E-value: 1.10e-82
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bfr | TIGR00754 | bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to ... |
1-157 | 1.55e-81 | |||
bacterioferritin; Bacterioferritin, predominantly an iron-storage protein restricted to Bacteria, has also been designated cytochrome b1 and cytochrome b-557.Bacterioferritin is a homomultimer most species. In Neisseria gonorrhoeae, Synechocystis PCC6803, Magnetospirillum magnetotacticum, and Pseudomonas aeruginosa, two types of subunit are found in a heteromultimeric complex, with each species having one member of each type. At present, both types of subunit are including in this single model. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 162022 Cd Length: 157 Bit Score: 237.40 E-value: 1.55e-81
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Ferritin | pfam00210 | Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ... |
8-143 | 1.64e-37 | |||
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins. Pssm-ID: 459712 Cd Length: 141 Bit Score: 125.09 E-value: 1.64e-37
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Ferritin_like | cd00657 | Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ... |
11-138 | 2.12e-15 | |||
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF). Pssm-ID: 153097 Cd Length: 130 Bit Score: 68.29 E-value: 2.12e-15
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DPSL | cd01052 | DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ... |
5-138 | 5.55e-06 | |||
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a phylogenetically distinct class within the ferritin-like superfamily, and similar in many ways to the DPS (DNA Protecting protein under Starved conditions) proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize hydrogen peroxide in the controlled oxidation of iron, and possess a short N-terminal extension implicated in stabilizing cellular DNA. This domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. These proteins are distantly related to bacterial ferritins which assemble 24 monomers, each of which have a four-helix bundle with a fifth shorter helix at the C terminus and a diiron (ferroxidase) center. Ferritins contain a center where oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of iron in the ferric form. Many of the conserved residues of a diiron center are present in this domain. Pssm-ID: 153111 Cd Length: 148 Bit Score: 43.82 E-value: 5.55e-06
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Dps | COG0783 | DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and ... |
5-131 | 5.86e-06 | |||
DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism, Defense mechanisms]; Pssm-ID: 440546 [Multi-domain] Cd Length: 156 Bit Score: 43.67 E-value: 5.86e-06
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Mn_catalase_like | cd07908 | Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ... |
18-138 | 6.26e-05 | |||
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF). Pssm-ID: 153117 Cd Length: 154 Bit Score: 40.72 E-value: 6.26e-05
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DPS | COG2406 | Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, ... |
5-145 | 9.06e-05 | |||
Ferritin-like DNA-binding protein, DPS (DNA Protection under Starvation) family [Replication, recombination and repair]; Pssm-ID: 441962 Cd Length: 165 Bit Score: 40.66 E-value: 9.06e-05
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DPS | cd01043 | DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved ... |
44-131 | 9.77e-04 | |||
DPS protein, ferritin-like diiron-binding domain; DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic. Pssm-ID: 153102 Cd Length: 139 Bit Score: 37.14 E-value: 9.77e-04
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